Common core structure of amyloid fibrils by synchrotron X-ray diffraction

Sunde, Margaret, Serpell, Louise C, Bartlam, Mark, Fraser, Paul E, Pepys, Mark B and Blake, Colin C F (1997) Common core structure of amyloid fibrils by synchrotron X-ray diffraction. Journal of Molecular Biology, 273 (3). pp. 729-739. ISSN 00222836

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Abstract

Tissue deposition of normally soluble proteins as insoluble amyloid fibrils is associated with serious diseases including the systemic amyloidoses, maturity onset diabetes, Alzheimer's disease and transmissible spongiform encephalopathy. Although the precursor proteins in different diseases do not share sequence homology or related native structure, the morphology and properties of all amyloid fibrils are remarkably similar. Using intense synchrotron sources we observed that six different ex vitro amyloid fibrils and two synthetic fibril preparations all gave similar high-resolution X-ray fibre diffraction patterns, consistent with a helical array of ß-sheets parallel to the fibre long axis, with the strands perpendicular to this axis. This confirms that amyloid fibrils comprise a structural superfamily and share a common protofilament substructure, irrespective of the nature of their precursor proteins.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Louise Serpell
Date Deposited: 06 Feb 2012 18:20
Last Modified: 30 Nov 2012 16:59
URI: http://sro.sussex.ac.uk/id/eprint/15878
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